Juridical Foundation the Chemo-sero-therapeutic Research Institute

Teijin Limited

Kowa Company Limited

The Chemo-sero-therapeutic Research Institute

Hiroshi Mizokami

Yoshinobu Miyatsu

Tetsuo Kawahara

Yoshitaka Tajima

Sadao Susumi

Fukusaburo Hamada

Tsukasa Nishihara

Akihiro Ginnaga

Toshinobu Nouchi

Kyosuke Mizuno

Toshihiro Maeda

Kazuyuki Nakashima

Satoshi Koyanagi

Shinichi Furukawa

Satoshi Adachi

Toshio Murakami

Seiichi Yokoyama

Masashi Sakaguchi

Hideo Yoshizaki

Hirofumi Higuchi

Nobuya Ohtomo

Mitsuo Sakoh

Yoshiharu Takazawa

Ryuichi Sakamoto

Keiichi Makizumi

Takami Arai

Shin Sakuma

Keishin Sugawara

Keishin Sugahara

Kenji Nagura

Kenjiro Kawatsu

Yoshitaka Ushio

Tomitaka Tashiro

Kou-ichi Shiosaki

Youichiro Kino

Tatsufumi Onchi

Masamichi Motoki

Kazuhiro Komatsu

Kazunari Yagi

Masahiro Sakaguchi

Tetsurou Tanabe

Shinichi Shibata

Susumu Baba

A recombinant avian infectious coryza vaccine and a process for preparing the same are provided. A process for preparing a recombinant avian infectious coryza vaccine which comprises step of constructingthat may produce as an inclusion body a fusion peptide consisting of peptides derived from outer-membrane protein ofserotype A and serotype C, step of culturing saidand collecting and purifying inclusion body from culture, and step of preparing a preparation comprising said purified inclusion body, and an avian infectious coryza vaccine comprising as an active ingredient the fusion peptide. A linker sequence may be inserted between the respective peptides comprising the fusion peptide. For the peptide derived from the serotypes A and C, an amino acid sequence region of Region 2 or its vicinity responsible for protection from infection may be used.

Recombinant avian infectious coryza vaccine and process for preparing same

A method of enhancing the efficacy of a monoclonal antibody preparation wherein antigens from patients are tested for their reactivity with the antibody. An amino acid sequence of an expressed protein is deuced from a nucleotide sequence determined by isolation and analysis of a target molecule gene in a biopsy from a patient. This is compared with the previously determined amino acid sequence recognized by the monoclonal antibody preparation in order to assess the fitness of patients for administration of the monoclonal antibody preparation.

Method for enhancing efficacy of preparation of monoclonal antibody

A method for purifying a modified major mite allergen obtained by the genetic recombination technique and a purified modified major mite allergen obtained by said method for purification are provided. A method for purifying a modified major mite allergen obtained by the genetic recombination technique, which comprises the purification steps: (1) Washing and recovering inclusion bodies containing a modified major mite allergen obtained by the genetic recombination technique with MF membrane; (2) Dissolving said inclusion bodies followed by refolding; (3) Concentrating a solution containing the modified major mite allergen with simultaneous removal of low molecular weight components with ultrafiltration membrane; (4) Recovering the modified major mite allergen in non-adsorbed fractions with an anion exchanger; (5) Recovering the modified major mite allergen in adsorbed fractions with a hydrophobic gel; and (6) Recovering the modified major mite allergen in adsorbed fractions with an anion exchanger, and a modified major mite allergen with high purity obtained by said method for purification.

Method for purifying modified major mite allergen

The present invention herein discloses a method for purifying human serum albumin, which is characterized in that it comprises the steps of heat-treating a human serum albumin-containing solution including impurities originated from a host cell, in the presence of a divalent cation such as calcium ion, magnesium ion, nickel ion, cobalt ion, iron ion and zinc ion to thus selectively allow the impurities to undergo agglutination. The present invention also provides the highly purified human serum albumin prepared by the foregoing method.

Method for preparing human serum albumin through heat-treatment in the presence of divalent cation

Multimers of human serum albumin are removed from a solution of human serum albumin containing the multimers by bringing the human serum albumin solution into contact with an anion-exchanger equilibrated with a buffer containing a salt in a concentration ranging from 10 to 150 mM and having a pH value ranging from 5 to 9.5.

Method for removing multimers of human serum albumin

A method for preparing human serum albumin comprises the step of heat-treating a human serum albumin solution containing contaminants at a pH value in the proximity to the isoelectric point of the contaminants.

Method for preparing human serum albumin containing heat-treatment

The present invention relates to a method for purifying a calcium ion-binding protein by cation exchange chromatography. The present invention provide a method for isolating and purifying a calcium ion-binding protein in a simple and efficient manner from a liquid sample containing a calcium ion-binding protein and contaminants without any pretreatment such as addition of a chelating agent. More specifically, the present invention relates to a method for purifying a calcium ion-binding protein which comprises contacting said protein with a cation exchange carrier in the presence of calcium ions to let the said protein be adsorbed to the carrier, and after washing, eluting said protein, and to a calcium ion-binding protein having substantially no contaminants obtained by the method of the present invention.

Method of purifying calcium ion-binding protein

The present invention provides a t-PA medicinal preparation obtained by remarkably improving the solubility and stability of t-PA or modified t-PA. Nicotinamide or a derivative thereof is incorporated into t-PA or modified t-PA-containing solvent system. If necessary, a citrate buffer solution is also used. The t-PA-containing medicinal composition is in the form of, for example, a freeze-dried preparation.

Tissue plasminogen activator medicinal composition

Medium for culturing animal cells

Improved method for the purification of LPF-HA (Leucocytosis promoting far hemagglutinin) on industrial scale which comprises contacting a LPF-HA-containing solution from culture media of Bordetella pertussis with a cellulose sulfate gel, a crosslinked polysaccharide sulfate gel, or a polysaccharide gel chemically bound with dextran sulfate, thereby adsorbing LPF-HA on the gel, and then eluting LPF-HA from the gel. Said method can give a highly purified LPF-HA which does not contain any other proteins, lipid, saccharides, etc. and further undesirable endotoxin, and hence can be used for producing various reagents, medicines and pertussis vaccine.

Method for the purification of LPF-HA

Industrially useful method for the purification of HBs antigen produced by a recombinant organism being capable of producing HBs antigen which is prepared by means of DNA recombination technique, which comprises subjecting an HBs antigen-containing material produced by a recombinant organism to an adsorption chromatography with a silica, optionally followed by a gel filtration and further an adsorption chromatography with a hydroxyapatite, and then eluting the HBs antigen, preferably, with a buffer having a pH 9 or more which is incorporated with urea. The purification method can give a highly pure HBs antigen suitable for the preparation of hepatitis B vaccine in a large scale from recombinant organisms prepared by DNA recombination technique.

Method for purification of HBs antigen

A method for the preparation of an herpes simplex virus subunit vaccine, which comprises subjecting a solution containing glycoproteins gA and gB to column chromatography using, as a gel for chromatography, sulfuric acid ester of cellulose or a crosslinked polysaccharide to adsorb the glycoproteins gA and gB onto the gel in the presence of an anionic surfactant or a nonanionic surfactant, eluting the adsorbed glycoproteins to obtain an eluate containing the glycoproteins, and subjecting the eluate to gel filtration to obtain a filtrate containing the glycoproteins.

Method for preparation herpes simplex virus subunit vaccine

Lyophilized preparation of hepartitis B vaccine, which comprises a purified hepatitis B virus surface antigen produced by a recombinant organism being capable of producing HBs antigen, which is adsorbed on aluminum gel in the lyophilized state in the presence of a stabilizer, said lyophilized preparation being prepared by the steps of adding an aluminum gel and a stabilizer to a purified recombinant-origin HBs antigen and lyophilizing the mixture. Said lyophilized preparation being able to be stably kept for a long period of time without losing its antigen titer and being useful for the prophylaxis of infection of hepatitis B virus.

Lyophilized hepatitis B vaccine

Improved method for the purification of filamentous hemagglutinin (F-HA) on industrial scale which comprises contacting a culture of a microorganism of the genus Bordetella with a cellulose sulfate gel, a polysaccharide gel chemically bound with dextran sulfate, or a crosslinked polysaccharide sulfate gel, thereby adsorbing F-HA on the gel, and then eluting F-HA from the gel. Said method can give a highly purified F-HA which does not contain any other proteins, lipid, saccharides, etc. and further undesirable endotoxin, and hence can be used for producing various reagents, medicines and pertussis vaccine.

Method for purification of filamentous hemagglutinin

An improved method for the purification of hepatitis B virus surface anti by column chromatography, which is characteristic in using as a gel for the chromatography a sulfuric acid ester of a crosslinked polysaccharide or cellulose which is obtained by sulfating a crosslinked polysaccharide or cellulose. Said method can give a highly purified hepatitis B virus surface antigen which is useful for the preparation of hepatitis B virus vaccine.

Method for purification of hepatitis B virus surface antigen

Growing community of inventors

Kikuchi, Japan

Hiroshi Mizokami